Evidence map›Paper›PMID 20534812›Full record

ArticleMolecular biology of the cell2010

Functional cross-talk between Rab14 and Rab4 through a dual effector, RUFY1/Rabip4.

Hideaki Yamamoto, Hiroshi Koga, Yohei Katoh, Senye Takahashi, Kazuhisa Nakayama, Hye-Won Shin

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
2.4field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

51 citing papers in PubMed, 69 citations in OpenAlex.

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  19. Ligand-bound integrin αvβ6 internalisation and trafficking.Frontiers in cell and developmental biology · 2022
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Hideaki YamamotoGraduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan.
Hiroshi Koga
Yohei Katoh
Senye Takahashi
Kazuhisa Nakayama
Hye-Won Shin
Kumamoto University · JPAlbert Einstein College of Medicine · USKyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The small GTPase Rab14 localizes to early endosomes and the trans-Golgi network, but its cellular functions on endosomes and its functional relationship with other endosomal Rab proteins are poorly understood. Here, we report that Rab14 binds in a GTP-dependent manner to RUFY1/Rabip4, which had been originally identified as a Rab4 effector. Rab14 colocalizes well with Rab4 on peripheral endosomes. Depletion of Rab14, but not Rab4, causes dissociation of RUFY1 from endosomal membranes. Coexpression of RUFY1 with either Rab14 or Rab4 induces clustering and enlargement of endosomes, whereas a RUFY1 mutant lacking the Rab4-binding region does not induce a significant morphological change in the endosomal structures even when coexpressed with Rab14 or Rab4. These findings suggest that Rab14 and Rab4 act sequentially, together with RUFY1; Rab14 is required for recruitment of RUFY1 onto endosomal membranes, and subsequent RUFY1 interaction with Rab4 may allow endosomal tethering and fusion. Depletion of Rab14 or RUFY1, as well as Rab4, inhibits efficient recycling of endocytosed transferrin, suggesting that Rab14 and Rab4 regulate endosomal functions through cooperative interactions with their dual effector, RUFY1.

Indexed as

Adaptor Proteins, Signal TransducingEndocytosisEndosomesGuanosine TriphosphateHeLa CellsHumansIntracellular MembranesIntracellular Signaling Peptides and ProteinsMutant ProteinsProtein BindingProtein Transportrab4 GTP-Binding Proteinsrab GTP-Binding ProteinsTransferrinAdaptor Proteins, Signal TransducingGuanosine TriphosphateIntracellular Signaling Peptides and ProteinsMutant ProteinsRab14 protein, humanrab4 GTP-Binding Proteinsrab GTP-Binding ProteinsRUFY1 protein, humanTransferrin

Identifiers

PMID20534812
PMCPMC2912359
OpenAlexW2156003554

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.